The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The target is human GET4 (synonyms TRC35, C7orf20, CEE, CGI-20), the metazoan homolog of yeast Get4, and a core component of the mammalian TRC/GET tail-anchored (TA) protein targeting pathway. This mapping is explicitly stated in comparative pathway literature that equates metazoan Get4 with TRC35 and cites UniProt Q7L5D6 in this context. (najdrova2022conservedmechanismfor pages 16-20, najdrova2022conservedmechanismfor pages 20-23)
TA proteins are single-pass membrane proteins whose hydrophobic transmembrane domain (TMD) is at the extreme C-terminus, so the targeting signal emerges only after translation terminates; therefore TA proteins are primarily handled by post-translational targeting systems. (najdrova2022conservedmechanismfor pages 88-98)
The GET pathway (yeast terminology) and TRC pathway (mammalian terminology) constitute a conserved cytosolic-to-ER relay that captures TA TMDs in the cytosol, loads them onto a targeting ATPase (Get3 in yeast; TRC40/ASNA1 in mammals), and delivers them to an ER membrane receptor/insertase (Get1/Get2 in yeast; WRB/CAML in mammals) for insertion. (najdrova2022conservedmechanismfor pages 16-20, farkas2021captureanddelivery pages 1-3)
GET4/TRC35 is not an enzyme and does not catalyze a chemical reaction. Its primary role is as a scaffold/adaptor in the pre-targeting complex that promotes client handoff to TRC40 and coordinates targeting vs quality-control decisions for hydrophobic clients. (pool2022targetingofproteins pages 7-9, keszei2021structuralinsightsinto pages 6-7)
Multiple reviews and structural studies converge on a mechanistic model in which GET4/TRC35 participates in the cytosolic pretargeting complex that connects upstream TA capture factors to the downstream targeting ATPase:
A key primary structural study defined the metazoan pretargeting GET complex architecture (cBUGG: cBag6–Ubl4a–Get4–Get3) and how it promotes substrate transfer:
These data support the current view that GET4/TRC35 is a noncatalytic organizational factor that enhances the efficiency and fidelity of TA handoff to TRC40/ASNA1. (keszei2021structuralinsightsinto pages 6-7)
In metazoans, yeast Get4/Get5 is replaced/augmented by a heterotrimeric complex containing BAG6, UBL4A (Get5 homolog), and TRC35/GET4. This complex is repeatedly described as central to TA biogenesis and transfer to TRC40. (najdrova2022conservedmechanismfor pages 16-20, mock2017structuralbasisfor pages 1-2)
GET4/TRC35 functions in the cytosol, early in the pathway, in a ribosome-proximal capture/transfer environment as described in reviews of ER targeting and TA biogenesis. (pool2022targetingofproteins pages 7-9, qin2023targetingandsurveillance pages 1-2)
A major human-specific mechanistic finding is that TRC35 directly regulates where BAG6 resides:
This provides a concrete mechanistic link between the TA targeting apparatus and cellular compartmentalization of a multifunctional cofactor (BAG6). (mock2017structuralbasisfor pages 1-2)
Beyond productive TA targeting, BAG6-containing complexes are described as mediating triage of exposed hydrophobic segments: substrates can be transferred to TRC40 for insertion or directed toward ubiquitin–proteasome degradation when targeting fails or clients are defective/mislocalized. (costa2017intracellulartargetingof pages 25-30, farkas2021captureanddelivery pages 1-3)
This contextualizes GET4/TRC35 as part of a network that couples membrane-protein biogenesis to proteostasis quality control. (pool2022targetingofproteins pages 7-9)
In human TRC35 biology, proper assembly with BAG6 affects TRC35 stability:
This supports a model in which GET4/TRC35 is itself surveilled by quality-control machinery, and correct complex assembly protects it. (mock2017structuralbasisfor pages 2-3)
Direct GET4/TRC35-focused primary literature in 2024 was limited in the accessible corpus for this run; however, 2023 studies provide meaningful, mechanistically relevant updates on the stress sensitivity and broader proteostasis integration of the BAG6–UBL4A–GET4 module.
A 2023 review summarizes the TRC/GET system as a conserved TA targeting route and reiterates the key role of the Get4/TRC35 pretargeting complex (with UBL4A, BAG6) in TA capture and transfer, emphasizing the integration of targeting with surveillance of mistargeted TA proteins. (qin2023targetingandsurveillance pages 1-2)
Publication: Qin et al. 2023-01, The Innovation Life. URL: https://doi.org/10.59717/j.xinn-life.2023.100013 (qin2023targetingandsurveillance pages 1-2)
A 2023 Biochemical Journal study tested how proteotoxic stresses affect complex integrity:
Publication: Hagiwara et al. 2023-10, Biochemical Journal. URL: https://doi.org/10.1042/bcj20230267 (hagiwara2023proteotoxicstressesstimulate pages 7-10)
A 2023 Nature paper (noncoding translation mitigation) identifies BAG6 pathway components including TRC35/GET4 in a broader proteostasis/surveillance context (as reported in the retrieved snippet), supporting the idea that GET4-containing modules participate not only in TA targeting but also in mitigation of aberrant translation-derived hydrophobic products. (OpenTargets Search: -GET4)
Publication: Kesner et al. 2023-04, Nature. URL: https://doi.org/10.1038/s41586-023-05946-4 (OpenTargets Search: -GET4)
In practice, GET4/TRC35 is used as a mechanistic handle to:
These applications are most mature in mechanistic cell biology and structural biology rather than direct clinical implementation.
Several authoritative reviews emphasize a consistent expert consensus:
Open Targets aggregates evidence connecting GET4 to several disease/phenotype terms, including neurodegenerative disease, atrial fibrillation, atrial flutter, and congenital disorder of glycosylation type IIy. These are associations drawn from specific studies/variants and functional screens, not proof of direct causality or a defined GET4 mechanism in each disease. (OpenTargets Search: -GET4)
Given that the BAG6–UBL4A–GET4 module is implicated in:
it is mechanistically plausible that perturbations could contribute to proteostasis-linked diseases, but the accessible primary clinical genetics evidence for GET4 specifically was limited in this run.
The cryo-EM figure extracted from Keszei et al. illustrates the cBUGG (cBag6–Ubl4a–Get4–Get3) architecture and how SGTA remodels it, supporting the “recruitment platform” concept for GET4/TRC35 function. (keszei2021structuralinsightsinto media 33007d62, keszei2021structuralinsightsinto media 2e1a5e15)
The following table consolidates identity, molecular function, partners, localization, QC roles, and key references.
| Entity / aspect | Summary for human GET4 / TRC35 | Key evidence / mechanism | Evidence type | Key references |
|---|---|---|---|---|
| Identity | GET4 encodes the human guided entry of tail-anchored proteins factor 4; common aliases include TRC35, C7orf20, CEE, and CGI-20. It is the metazoan homolog of yeast Get4 and matches the UniProt target Q7L5D6 discussed in the GET/TRC literature (najdrova2022conservedmechanismfor pages 16-20, najdrova2022conservedmechanismfor pages 20-23). | Conserved assignment of metazoan Get4 to TRC35/GET4 in reviews and comparative pathway analyses (najdrova2022conservedmechanismfor pages 16-20, najdrova2022conservedmechanismfor pages 20-23). | Comparative pathway mapping, review | Qin 2023, The Innovation Life, doi: https://doi.org/10.59717/j.xinn-life.2023.100013 ; Pool 2022, IJMS, doi: https://doi.org/10.3390/ijms23073773 |
| Primary molecular function | GET4/TRC35 is a cytosolic pretargeting scaffold/adaptor in the GET/TRC pathway for tail-anchored (TA) membrane proteins. It does not catalyze a chemical reaction; instead, it helps organize factors that capture, shield, and hand off hydrophobic TA transmembrane domains to the targeting ATPase TRC40/ASNA1 for ER delivery (pool2022targetingofproteins pages 7-9, shan2019guidingtailanchoredmembrane pages 2-4, najdrova2022conservedmechanismfor pages 16-20, keszei2021structuralinsightsinto pages 6-7). | Reviews and structural work place Get4/TRC35 in the upstream relay between SGTA/Sgt2 and Get3/TRC40, promoting efficient substrate loading onto the ATPase (pool2022targetingofproteins pages 7-9, shan2019guidingtailanchoredmembrane pages 2-4, keszei2021structuralinsightsinto pages 6-7). | Review, biochemical, cryo-EM | Shan 2019, JBC, doi: https://doi.org/10.1074/jbc.rev119.006197 ; Keszei 2021, Nat Struct Mol Biol, doi: https://doi.org/10.1038/s41594-021-00690-7 |
| Core complex composition | In mammals, GET4/TRC35 is a stable component of the BAG6–UBL4A–GET4 pretargeting complex (often treated as the metazoan counterpart of yeast Get4/Get5). BAG6 binds both GET4/TRC35 and UBL4A/Get5; SGTA acts upstream in TA capture; TRC40/ASNA1 is the downstream targeting ATPase; ER insertion is completed at WRB/CAML (costa2017intracellulartargetingof pages 25-30, najdrova2022conservedmechanismfor pages 16-20, mock2017structuralbasisfor pages 1-2, farkas2021captureanddelivery pages 1-3). | Human/metazoan studies and reviews describe a heterotrimeric BAG6–UBL4A–TRC35 complex that receives TA substrates from SGTA and transfers them to TRC40 for delivery to WRB/CAML (mock2017structuralbasisfor pages 1-2, farkas2021captureanddelivery pages 1-3). | Structural, biochemical, review | Mock 2017, PNAS, doi: https://doi.org/10.1073/pnas.1702940114 ; Farkas & Bohnsack 2021, J Cell Biol, doi: https://doi.org/10.1083/jcb.202105004 |
| Mechanistic role in TA targeting: capture and handoff | Canonical handoff sequence: ribosome / chaperones → SGTA → BAG6–UBL4A–GET4(TRC35) → TRC40/ASNA1 → WRB/CAML at the ER. GET4/TRC35 helps create the recruitment platform that positions upstream factors for TA substrate transfer to Get3/TRC40; in metazoan cryo-EM, UBL4A-cBAG6-GET4 forms a recruitment platform above the Get3 substrate chamber (keszei2021structuralinsightsinto pages 6-7, keszei2021structuralinsightsinto media 33007d62). | Keszei et al. defined a metazoan pretargeting architecture where Get4 helps position Ubl4a/BAG6 to recruit SGTA and promote substrate transfer; mutations affecting the secondary Get3–Get4 interface impaired SGTA→Get3 transfer without blocking Get3 substrate capture per se (keszei2021structuralinsightsinto pages 6-7). | Cryo-EM, crosslinking, biochemical | Keszei 2021, Nat Struct Mol Biol, doi: https://doi.org/10.1038/s41594-021-00690-7 ; Figure context (keszei2021structuralinsightsinto media 33007d62) |
| Ribosome association / early targeting stage | GET4/TRC35 functions early, close to the site of synthesis. Reviews describe the mammalian pretargeting machinery as ribosome-associated or ribosome-proximal, with TA capture occurring at or near the ribosome before handoff to TRC40; Get4/TRC35 was also identified among ribosome-associated proteins in comparative analyses (pool2022targetingofproteins pages 7-9, qin2023targetingandsurveillance pages 1-2, najdrova2022conservedmechanismfor pages 20-23). | Pool 2022 describes TRC35 within ribosome-associated BAG6 complexes; Qin 2023 discusses ribosome-proximal capture and competition near the tunnel exit; comparative analysis notes Get4 identification in ribosome-associated screens (pool2022targetingofproteins pages 7-9, qin2023targetingandsurveillance pages 1-2, najdrova2022conservedmechanismfor pages 20-23). | Review, proteomic / comparative inference | Pool 2022, IJMS, doi: https://doi.org/10.3390/ijms23073773 ; Qin 2023, The Innovation Life, doi: https://doi.org/10.59717/j.xinn-life.2023.100013 |
| Subcellular localization | Best-supported localization is cytosolic, within the pretargeting complex acting before ER membrane insertion. Functionally, GET4/TRC35 is linked to ER targeting through its interaction network, but it is not itself the ER insertase; ER insertion is mediated by WRB/CAML after TRC40 delivery (najdrova2022conservedmechanismfor pages 16-20, mock2017structuralbasisfor pages 1-2, farkas2021captureanddelivery pages 1-3). | Cytosolic pretargeting role is consistently reported in reviews and structural studies; downstream localization step is ER membrane insertion by WRB/CAML, not by GET4 itself (najdrova2022conservedmechanismfor pages 16-20, mock2017structuralbasisfor pages 1-2, farkas2021captureanddelivery pages 1-3). | Review, structural | Mock 2017, PNAS, doi: https://doi.org/10.1073/pnas.1702940114 ; Farkas & Bohnsack 2021, J Cell Biol, doi: https://doi.org/10.1083/jcb.202105004 |
| Control of BAG6 nucleo-cytoplasmic distribution | A key human-specific mechanistic finding is that TRC35 masks the BAG6 nuclear localization sequence (NLS), thereby retaining BAG6 in the cytosol. Overexpression of TRC35 increases cytosolic retention of BAG6; structural analysis showed TRC35 occludes the first basic cluster of the BAG6 NLS (mock2017structuralbasisfor pages 1-2, mock2017structuralbasisfor pages 2-3). | Human crystal structure and biochemical assays support direct Bag6–TRC35 interfaces; buried surface metrics and mutational effects showed that physiological complex assembly regulates BAG6 localization (mock2017structuralbasisfor pages 1-2, mock2017structuralbasisfor pages 2-3). | Crystal structure, biochemical, cell biology | Mock 2017, PNAS, doi: https://doi.org/10.1073/pnas.1702940114 |
| Quality control role: substrate triage | GET4/TRC35 participates in a module that links TA targeting with cytosolic quality control. BAG6-containing complexes can direct hydrophobic or mislocalized clients either toward productive loading onto TRC40 or toward ubiquitin-proteasome degradation, helping prevent aggregation of exposed transmembrane segments (pool2022targetingofproteins pages 7-9, costa2017intracellulartargetingof pages 25-30, farkas2021captureanddelivery pages 1-3, hagiwara2023proteotoxicstressesstimulate pages 1-3). | Reviews emphasize the dual targeting-versus-degradation role of BAG6 complexes; Hagiwara 2023 further links this machinery to aggregate/proteotoxic stress responses (farkas2021captureanddelivery pages 1-3, hagiwara2023proteotoxicstressesstimulate pages 1-3). | Review, biochemical | Farkas & Bohnsack 2021, J Cell Biol, doi: https://doi.org/10.1083/jcb.202105004 ; Hagiwara 2023, Biochem J, doi: https://doi.org/10.1042/bcj20230267 |
| Quality control role: RNF126 and TRC35 stability | Human studies indicate that unassembled or mutant TRC35 can become a target of RNF126-mediated ubiquitylation in the BAG6-associated quality-control network. Proper Bag6 association protects TRC35; Bag6-disrupting mutants increased Ub-conjugated TRC35 and lowered steady-state TRC35 levels, reversible by proteasome inhibition (MG132) (mock2017structuralbasisfor pages 2-3). | Mock et al. identified RNF126 as a Bag6-associated E3 ligase implicated in TRC35 ubiquitylation and showed that disrupted physiological Bag6–TRC35 interaction destabilizes TRC35 (mock2017structuralbasisfor pages 2-3). | Structural, biochemical, ubiquitination assay | Mock 2017, PNAS, doi: https://doi.org/10.1073/pnas.1702940114 |
| Proteotoxic stress effects (2023) | In 2023, proteotoxic stress studies showed that the TA recognition complex is stress-sensitive: polyQ aggregates, proteasome inhibition, and CCCP-induced mitochondrial depolarization promoted dissociation of UBL4A from BAG6, implying that the BAG6–UBL4A–GET4 module is remodeled under proteotoxic conditions and may shift away from normal TA biogenesis (hagiwara2023proteotoxicstressesstimulate pages 7-10, hagiwara2023proteotoxicstressesstimulate pages 1-3). | Hagiwara et al. reported quantitative assays: co-IP with n = 6 biological replicates analyzed by Student’s t-test; NanoBiT CCCP time-course n = 3, P < 0.01; CCCP 4 h assay n = 4, Welch’s t-test, P < 0.01 (hagiwara2023proteotoxicstressesstimulate pages 7-10). | Biochemical, cell assay, quantitative stress biology | Hagiwara 2023, Biochem J, doi: https://doi.org/10.1042/bcj20230267 |
| Related nuclear / DNA-damage context | The strongest direct evidence concerns BAG6, not GET4 as an autonomous nuclear factor. Because TRC35 controls BAG6 cytosolic retention, it indirectly interfaces with BAG6’s reported nuclear functions in p300 acetylation, histone methylation, and DNA-damage signaling-mediated cell death; however, direct GET4-specific nuclear signaling functions remain less established than its pretargeting role (mock2017structuralbasisfor pages 1-2). | Mock 2017 explicitly ties TRC35 to BAG6 localization control while noting BAG6 nuclear functions; evidence is indirect for GET4 beyond localization control (mock2017structuralbasisfor pages 1-2). | Structural, cell biology, literature synthesis | Mock 2017, PNAS, doi: https://doi.org/10.1073/pnas.1702940114 |
| 2023–2024 broader relevance / applications | Recent literature places GET4/TRC35-containing BAG6 complexes in broader proteostasis surveillance, including mitigation of aberrant noncoding translation products and maintenance of membrane protein biogenesis fidelity. One 2023 Nature study identified BAG6, TRC35/GET4, RNF126, SGTA, and UBL4A in this surveillance axis (OpenTargets Search: -GET4). Disease links in Open Targets are currently association-level rather than definitive mechanism-level annotations for GET4 itself (OpenTargets Search: -GET4). | Evidence supports translational quality control relevance but not yet a mature clinical application directly targeting GET4; Open Targets associations include neurodegenerative disease and congenital disorder of glycosylation type IIy, but these should be interpreted cautiously as evidence aggregation rather than causal proof (OpenTargets Search: -GET4). | Genetics / CRISPRi association, database aggregation | Kesner 2023, Nature, doi: https://doi.org/10.1038/s41586-023-05946-4 ; Open Targets context (OpenTargets Search: -GET4) |
Table: This table summarizes the best-supported functions, interactions, localization, quality-control roles, and recent developments for human GET4/TRC35 (UniProt Q7L5D6). It emphasizes experimentally grounded mechanisms in tail-anchored protein targeting and distinguishes direct evidence from broader association-level disease links.
Human GET4/TRC35 (UniProt Q7L5D6) is a conserved, cytosolic, ribosome-proximal pretargeting scaffold in the TRC/GET pathway that promotes handoff of nascent tail-anchored membrane proteins from SGTA to the targeting ATPase TRC40/ASNA1, enabling delivery to the ER insertase WRB/CAML. Its best-supported additional roles are in proteostasis-linked triage (via the BAG6 module), including regulation of BAG6 localization through NLS masking and stabilization of TRC35 by preventing inappropriate RNF126/proteasome-mediated degradation of unassembled TRC35; and the complex is stress-sensitive, with proteotoxic insults promoting dissociation of UBL4A–BAG6 interactions. (mock2017structuralbasisfor pages 1-2, keszei2021structuralinsightsinto pages 6-7, pool2022targetingofproteins pages 7-9, mock2017structuralbasisfor pages 2-3, hagiwara2023proteotoxicstressesstimulate pages 7-10)
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